Dengue virus PrM/M proteins fail to show pH-dependent ion channel activity in Xenopus oocytes
| Autor: | Bruce E. Loveland, Gholamreza Haqshenas, Sook-San Wong, Mary Chebib, Eric J. Gowans |
|---|---|
| Rok vydání: | 2011 |
| Předmět: |
Patch-Clamp Techniques
M protein Voltage clamp viruses Xenopus Dengue virus medicine.disease_cause Epitope law.invention Viral Proteins Xenopus laevis law Virology medicine Animals Lipid bilayer Ion channel Xenopus oocytes biology PrM virus diseases Hydrogen-Ion Concentration biology.organism_classification Molecular biology Transmembrane domain Ion channels Oocytes Recombinant DNA Female |
| Zdroj: | Virology. 412(1):83-90 |
| ISSN: | 0042-6822 |
| DOI: | 10.1016/j.virol.2010.12.050 |
| Popis: | The transmembrane domains (TMDs) of dengue virus type-1 M protein (DENV-1M) were reported to form cation-selective channels in artificial lipid bilayers. We further explored this observation using the two-electrode voltage clamp (TEVC) method on the Xenopus laevis oocytes expressing DENV PrM and M proteins. Using myc epitope tagged M proteins, M was first shown to adopt its predicted native topology in mammalian cells when expressed on its own. The recombinant proteins were then successfully expressed on the surface of Xenopus oocytes. Using influenza A M2 (Inf A/M2) protein as a control, we measured the conductance of oocytes expressing DENV proteins under hyperpolarized or low-pH conditions. Inf A/M2 showed pH-dependent, amantadine-sensitive channel activity that was consistent with previously published reports. However, no activity was detected for DENV proteins. We conclude that DENV PrM and M proteins do not show pH-activated ion channel activity. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect